Reviewed, UniProtKB/Swiss-Prot P16615 (AT2A2_HUMAN)

Names and origin

Protein names

Recommended name:
    Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
      Short name=SR Ca(2+)-ATPase 2
      Short name=SERCA2
    EC=3.6.3.8
Alternative name(s):
    Calcium pump 2
    Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform
    Endoplasmic reticulum class 1/2 Ca(2+) ATPase

Gene names

Name:	ATP2A2
Synonyms:	ATP2B

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1042 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Isoform SERCA2A is involved in the regulation of the contraction/relaxation cycle.
Catalytic activity	ATP + H2O + Ca2+(Cis) = ADP + phosphate + Ca2+(Trans).
Enzyme regulation	Reversibly inhibited by phospholamban (PLN) at low calcium concentrations. Dephosphorylated PLN decreases the apparent affinity of the ATPase for calcium. This inhibition is regulated by the phosphorylation of PLN By similarity.
Subunit structure	Associated with phospholamban (PLN) By similarity. Isoform SERCA2B interacts with TRAM2 (via C-terminus). Interacts with HAX1. Ref.3 Ref.10
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Sarcoplasmic reticulum membrane; Multi-pass membrane protein.
Tissue specificity	Isoform SERCA2A is highly expressed in heart and slow twitch skeletal muscle. Isoform SERCA2B is widely expressed, in smooth muscle and nonmuscle tissues such as in adult skin epidermis. Ref.14
Post-translational modification	Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity.
Involvement in disease	Defects in ATP2A2 are a cause of acrokeratosis verruciformis (AKV) [MIM:101900]; also known as Hopf disease. AKV is a localized disorder of keratinization, which is inherited as an autosomal dominant trait. Its onset is early in life with multiple flat-topped, flesh-colored papules on the hands and feet, punctate keratoses on the palms and soles, with varying degrees of nail involvement. The histopathology shows a distinctive pattern of epidermal features with hyperkeratosis, hypergranulosis, and acanthosis together with papillomatosis. These changes are frequently associated with circumscribed elevations of the epidermis that are said to resemble church spires. There are no features of dyskeratosis or acantholysis, the typical findings in lesions of Darier disease. Ref.17 Defects in ATP2A2 are the cause of Darier disease (DD) [MIM:124200]; also known as Darier-White disease (DAR). DD is an autosomal dominantly inherited skin disorder characterized by loss of adhesion between epidermal cells (acantholysis) and abnormal keratinization. Patients with mild disease may have no more than a few scattered keratotic papules or subtle nail changes, whereas those with severe disease are handicapped by widespread malodorous keratotic plaques. In a few families, neuropsychiatric abnormalities such as mild mental retardation, schizophrenia, bipolar disorder and epilepsy have been reported. Stress, UV exposure, heat, sweat, friction, and oral contraception exacerbate disease symptoms. Prevalence has been estimated at 1 in 50000. Ref.14 Ref.13 Ref.15 Ref.16
Sequence similarities	Belongs to the cation transport ATPase (P-type) family. Type IIA subfamily.

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Endoplasmic reticulum Membrane Sarcoplasmic reticulum
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Epilepsy
Domain	Transmembrane
Ligand	ATP-binding Calcium Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Acetylation Isopeptide bond Nitration Phosphoprotein Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro cell adhesion Ref.16 Traceable author statement. Source: ProtInc epidermis development Ref.16 Traceable author statement. Source: ProtInc sarcoplasmic reticulum calcium ion transport Traceable author statement. Source: UniProtKB
Cellular component	integral to plasma membrane Ref.1 Traceable author statement. Source: ProtInc microsome Ref.1 Traceable author statement. Source: ProtInc sarcoplasmic reticulum membrane Traceable author statement. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW S100 alpha binding Inferred from physical interaction. Source: UniProtKB calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW calcium-transporting ATPase activity Ref.1 Traceable author statement. Source: ProtInc magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein C-terminus binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PTP4A3	O75365	1	EBI-358933,EBI-1043866

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: SERCA2 transcripts differ only in their 3'-UTR region and are expressed in a tissue-specific manner.

Isoform SERCA2B (identifier: P16615-1)

Also known as: ATP2A2B; Class 2-4; HK1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: Ubiquitous housekeeping isoform.

Isoform SERCA2A (identifier: P16615-2)

Also known as: ATP2A2A; Class 1; HK2;

The sequence of this isoform differs from the canonical sequence as follows:
     994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → AILE

Note: Cardiac/slow twitch, muscle specific isoform. Has a lower affinity for calcium and a higher catalytic turnover rate.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1042	1042	Sarcoplasmic/endoplasmic reticulum calcium ATPase 2		PRO_0000046196
Regions
	Topological domain	1 – 48	48	Cytoplasmic By similarity
	Transmembrane	49 – 69	21	1 By similarity
	Topological domain	70 – 89	20	Lumenal By similarity
	Transmembrane	90 – 110	21	2 By similarity
	Topological domain	111 – 253	143	Cytoplasmic By similarity
	Transmembrane	254 – 273	20	3 By similarity
	Topological domain	274 – 295	22	Lumenal By similarity
	Transmembrane	296 – 313	18	4 By similarity
	Topological domain	314 – 756	443	Cytoplasmic By similarity
	Transmembrane	757 – 776	20	5 By similarity
	Topological domain	777 – 786	10	Lumenal By similarity
	Transmembrane	787 – 807	21	6 By similarity
	Topological domain	808 – 827	20	Cytoplasmic By similarity
	Transmembrane	828 – 850	23	7 By similarity
	Topological domain	851 – 896	46	Lumenal By similarity
	Transmembrane	897 – 916	20	8 By similarity
	Topological domain	917 – 929	13	Cytoplasmic By similarity
	Transmembrane	930 – 948	19	9 By similarity
	Topological domain	949 – 963	15	Lumenal By similarity
	Transmembrane	964 – 984	21	10 By similarity
	Topological domain	985 – 1042	58	Cytoplasmic By similarity
	Region	370 – 400	31	Interacts with phospholamban 1 By similarity
	Region	575 – 594	20	Interacts with HAX1
	Region	787 – 807	21	Interacts with phospholamban 2 By similarity
Sites
	Active site	351	1	4-aspartylphosphate intermediate By similarity
	Metal binding	304	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	305	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	307	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	309	1	Calcium 2 By similarity
	Metal binding	702	1	Magnesium By similarity
	Metal binding	706	1	Magnesium By similarity
	Metal binding	767	1	Calcium 1 By similarity
	Metal binding	770	1	Calcium 1 By similarity
	Metal binding	795	1	Calcium 2 By similarity
	Metal binding	798	1	Calcium 1 By similarity
	Metal binding	799	1	Calcium 1 By similarity
	Metal binding	799	1	Calcium 2 By similarity
	Metal binding	907	1	Calcium 1 By similarity
Amino acid modifications
	Modified residue	294	1	Nitrated tyrosine Ref.5
	Modified residue	295	1	Nitrated tyrosine Ref.5
	Modified residue	464	1	N6-acetyllysine Ref.12
	Modified residue	537	1	Phosphothreonine By similarity
	Modified residue	663	1	Phosphoserine Ref.4 Ref.6 Ref.7 Ref.8 Ref.11
	Cross-link	143		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Natural variations
	Alternative sequence	994 – 1042	49	GKECV…DMFWS → AILE in isoform SERCA2A.		VSP_000358
	Natural variant	23	1	G → E in DD. dbSNP rs28929478. Ref.16		VAR_008608
	Natural variant	39	1	N → T in DD. Ref.15		VAR_008609
	Natural variant	47	1	K → KMFLTGK in DD.		VAR_008610
	Natural variant	65	1	L → S in DD; severe form.		VAR_008611
	Natural variant	131	1	R → Q in DD.		VAR_008612
	Natural variant	160	1	P → L in DD.		VAR_008613
	Natural variant	186	1	S → P in DD.		VAR_008614
	Natural variant	211	1	G → D in DD; severe form.		VAR_008615
	Natural variant	223	1	V → M in DD.		VAR_008616
	Natural variant	268	1	C → F in DD; haemorrhagic lesions.		VAR_008617
	Natural variant	310	1	G → V in DD.		VAR_008618
	Natural variant	318	1	C → R in DD; severe form.		VAR_008619
	Natural variant	348	1	I → T in DD.		VAR_008620
	Natural variant	357	1	T → K in DD. Ref.16		VAR_009508
	Natural variant	412	1	E → G in DD.		VAR_008621
	Natural variant	495	1	S → F in DD. Ref.16		VAR_008622
	Natural variant	560	1	C → R in DD; neuropsychiatric phenotype. Ref.15		VAR_008623
	Natural variant	602	1	P → L in AKV; loss of activity. Ref.17		VAR_017532
	Natural variant	675	1	F → S in DD; multiple neuropsychiatric features.		VAR_008624
	Natural variant	683	1	K → E in DD; depression.		VAR_008625
	Natural variant	702	1	D → N in DD; moderate form.		VAR_008626
	Natural variant	745	1	A → D in DD; moderate form.		VAR_008627
	Natural variant	749	1	G → R in DD. Ref.16		VAR_009509
	Natural variant	754	1	Missing in DD.		VAR_008628
	Natural variant	765	1	S → L in DD. Ref.15		VAR_008629
	Natural variant	767	1	N → S in DD; haemorrhagic lesions and neuropsychiatric phenotype.		VAR_008630
	Natural variant	769	1	G → R in DD.		VAR_008631
	Natural variant	803	1	A → T in DD; mild/moderate form.		VAR_008632
	Natural variant	838	1	A → P in DD; severe form; petit mal epilepsy.		VAR_008633
	Natural variant	843	1	V → F in DD; depression.		VAR_008634
	Natural variant	875	1	C → G in DD; retinitis pigmentosa.		VAR_008635
	Natural variant	920	1	S → Y in DD; mild/moderate/severe form; one patient with epilepsy.		VAR_008636
	Natural variant	943	1	H → R in DD; learning difficulties.		VAR_008637
	Natural variant	975	1	P → R in DD.		VAR_008638

Sequences

	Sequence		Length	Mass (Da)
	Isoform SERCA2B (ATP2A2B) (Class 2-4) (HK1) [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 5462FF2DA7FB630A	FASTA	1,042	114,757
	10 20 30 40 50 60 MENAHTKTVE EVLGHFGVNE STGLSLEQVK KLKERWGSNE LPAEEGKTLL ELVIEQFEDL 70 80 90 100 110 120 LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILVA NAIVGVWQER NAENAIEALK 130 140 150 160 170 180 EYEPEMGKVY RQDRKSVQRI KAKDIVPGDI VEIAVGDKVP ADIRLTSIKS TTLRVDQSIL 190 200 210 220 230 240 TGESVSVIKH TDPVPDPRAV NQDKKNMLFS GTNIAAGKAM GVVVATGVNT EIGKIRDEMV 250 260 270 280 290 300 ATEQERTPLQ QKLDEFGEQL SKVISLICIA VWIINIGHFN DPVHGGSWIR GAIYYFKIAV 310 320 330 340 350 360 ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ 370 380 390 400 410 420 MSVCRMFILD RVEGDTCSLN EFTITGSTYA PIGEVHKDDK PVNCHQYDGL VELATICALC 430 440 450 460 470 480 NDSALDYNEA KGVYEKVGEA TETALTCLVE KMNVFDTELK GLSKIERANA CNSVIKQLMK 490 500 510 520 530 540 KEFTLEFSRD RKSMSVYCTP NKPSRTSMSK MFVKGAPEGV IDRCTHIRVG STKVPMTSGV 550 560 570 580 590 600 KQKIMSVIRE WGSGSDTLRC LALATHDNPL RREEMHLEDS ANFIKYETNL TFVGCVGMLD 610 620 630 640 650 660 PPRIEVASSV KLCRQAGIRV IMITGDNKGT AVAICRRIGI FGQDEDVTSK AFTGREFDEL 670 680 690 700 710 720 NPSAQRDACL NARCFARVEP SHKSKIVEFL QSFDEITAMT GDGVNDAPAL KKAEIGIAMG 730 740 750 760 770 780 SGTAVAKTAS EMVLADDNFS TIVAAVEEGR AIYNNMKQFI RYLISSNVGE VVCIFLTAAL 790 800 810 820 830 840 GFPEALIPVQ LLWVNLVTDG LPATALGFNP PDLDIMNKPP RNPKEPLISG WLFFRYLAIG 850 860 870 880 890 900 CYVGAATVGA AAWWFIAADG GPRVSFYQLS HFLQCKEDNP DFEGVDCAIF ESPYPMTMAL 910 920 930 940 950 960 SVLVTIEMCN ALNSLSENQS LLRMPPWENI WLVGSICLSM SLHFLILYVE PLPLIFQITP 970 980 990 1000 1010 1020 LNVTQWLMVL KISLPVILMD ETLKFVARNY LEPGKECVQP ATKSCSFSAC TDGISWPFVL 1030 1040 LIMPLVIWVY STDTNFSDMF WS
	Isoform SERCA2A (ATP2A2A) (Class 1) (HK2). Checksum: DD57D12A2B24FEC1	FASTA	997	109,691
	10 20 30 40 50 60 MENAHTKTVE EVLGHFGVNE STGLSLEQVK KLKERWGSNE LPAEEGKTLL ELVIEQFEDL 70 80 90 100 110 120 LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILVA NAIVGVWQER NAENAIEALK 130 140 150 160 170 180 EYEPEMGKVY RQDRKSVQRI KAKDIVPGDI VEIAVGDKVP ADIRLTSIKS TTLRVDQSIL 190 200 210 220 230 240 TGESVSVIKH TDPVPDPRAV NQDKKNMLFS GTNIAAGKAM GVVVATGVNT EIGKIRDEMV 250 260 270 280 290 300 ATEQERTPLQ QKLDEFGEQL SKVISLICIA VWIINIGHFN DPVHGGSWIR GAIYYFKIAV 310 320 330 340 350 360 ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ 370 380 390 400 410 420 MSVCRMFILD RVEGDTCSLN EFTITGSTYA PIGEVHKDDK PVNCHQYDGL VELATICALC 430 440 450 460 470 480 NDSALDYNEA KGVYEKVGEA TETALTCLVE KMNVFDTELK GLSKIERANA CNSVIKQLMK 490 500 510 520 530 540 KEFTLEFSRD RKSMSVYCTP NKPSRTSMSK MFVKGAPEGV IDRCTHIRVG STKVPMTSGV 550 560 570 580 590 600 KQKIMSVIRE WGSGSDTLRC LALATHDNPL RREEMHLEDS ANFIKYETNL TFVGCVGMLD 610 620 630 640 650 660 PPRIEVASSV KLCRQAGIRV IMITGDNKGT AVAICRRIGI FGQDEDVTSK AFTGREFDEL 670 680 690 700 710 720 NPSAQRDACL NARCFARVEP SHKSKIVEFL QSFDEITAMT GDGVNDAPAL KKAEIGIAMG 730 740 750 760 770 780 SGTAVAKTAS EMVLADDNFS TIVAAVEEGR AIYNNMKQFI RYLISSNVGE VVCIFLTAAL 790 800 810 820 830 840 GFPEALIPVQ LLWVNLVTDG LPATALGFNP PDLDIMNKPP RNPKEPLISG WLFFRYLAIG 850 860 870 880 890 900 CYVGAATVGA AAWWFIAADG GPRVSFYQLS HFLQCKEDNP DFEGVDCAIF ESPYPMTMAL 910 920 930 940 950 960 SVLVTIEMCN ALNSLSENQS LLRMPPWENI WLVGSICLSM SLHFLILYVE PLPLIFQITP 970 980 990 LNVTQWLMVL KISLPVILMD ETLKFVARNY LEPAILE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of cDNAs from human kidney coding for two alternatively spliced products of the cardiac Ca2+-ATPase gene." Lytton J., Maclennan D.H. J. Biol. Chem. 263:15024-15031(1988) [PubMed: 2844796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS SERCA2A AND SERCA2B). Tissue: Kidney.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SERCA2B). Tissue: Eye.
[3]	"TRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b and is necessary for collagen type I synthesis." Stefanovic B., Stefanovic L., Schnabl B., Bataller R., Brenner D.A. Mol. Cell. Biol. 24:1758-1768(2004) [PubMed: 14749390] [Abstract] Cited for: INTERACTION WITH TRAM2.
[4]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, MASS SPECTROMETRY. Tissue: Epithelium.
[5]	"Detection of sequence-specific tyrosine nitration of manganese SOD and SERCA in cardiovascular disease and aging." Xu S., Ying J., Jiang B., Guo W., Adachi T., Sharov V., Lazar H., Menzoian J., Knyushko T.V., Bigelow D., Schoeneich C., Cohen R.A. Am. J. Physiol. 290:H2220-H2227(2006) [PubMed: 16399855] [Abstract] Cited for: NITRATION AT TYR-294 AND TYR-295.
[6]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, MASS SPECTROMETRY. Tissue: Epithelium.
[7]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, MASS SPECTROMETRY.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, MASS SPECTROMETRY.
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]	"The anti-apoptotic protein HAX-1 interacts with SERCA2 and regulates its protein levels to promote cell survival." Vafiadaki E., Arvanitis D.A., Pagakis S.N., Papalouka V., Sanoudou D., Kontrogianni-Konstantopoulos A., Kranias E.G. Mol. Biol. Cell 20:306-318(2009) [PubMed: 18971376] [Abstract] Cited for: INTERACTION WITH HAX1.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, MASS SPECTROMETRY. Tissue: T-cell.
[12]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-464, MASS SPECTROMETRY.
[13]	"Spectrum of novel ATP2A2 mutations in patients with Darier's disease." Sakuntabhai A., Burge S., Monk S., Hovnanian A. Hum. Mol. Genet. 8:1611-1619(1999) [PubMed: 10441323] [Abstract] Cited for: VARIANTS DD.
[14]	"ATP2A2 mutations in Darier's disease: variant cutaneous phenotypes are associated with missense mutations, but neuropsychiatric features are independent of mutation class." Ruiz-Perez V.L., Carter S.A., Healy E., Todd C., Rees J.L., Steijlen P.M., Carmichael A.J., Lewis H.M., Hohl D., Itin P., Vahlquist A., Gobello T., Mazzanti C., Reggazini R., Nagy G., Munro C.S., Strachan T. Hum. Mol. Genet. 8:1621-1630(1999) [PubMed: 10441324] [Abstract] Cited for: VARIANTS DD, TISSUE SPECIFICITY.
[15]	"ATP2A2 mutations in Darier's disease and their relationship to neuropsychiatric phenotypes." Jacobsen N.J.O., Lyons I., Hoogendoorn B., Burge S., Kwok P.-Y., O'Donovan M.C., Craddock N., Owen M.J. Hum. Mol. Genet. 8:1631-1636(1999) [PubMed: 10441325] [Abstract] Cited for: VARIANTS DD THR-39; ARG-560 AND LEU-765.
[16]	"Mutations in ATP2A2, encoding a Ca2+ pump, cause Darier disease." Sakuntabhai A., Ruiz-Perez V., Carter S., Jacobsen N., Burge S., Monk S., Smith M., Munro C.S., O'Donovan M.C., Craddock N., Kucherlapati R., Rees J.L., Owen M.J., Lathrop G.M., Monaco A.P., Strachan T., Hovnanian A. Nat. Genet. 21:271-277(1999) [PubMed: 10080178] [Abstract] Cited for: VARIANTS DD GLU-23; LYS-357; PHE-495 AND ARG-749.
[17]	"Acrokeratosis verruciformis of Hopf is caused by mutation in ATP2A2: evidence that it is allelic to Darier's disease." Dhitavat J., Macfarlane S., Dode L., Leslie N., Sakuntabhai A., MacSween R., Saihan E., Hovnanian A. J. Invest. Dermatol. 120:229-232(2003) [PubMed: 12542527] [Abstract] Cited for: VARIANT AKV LEU-602.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	M23114 mRNA. Translation: AAA53193.1. M23116 Genomic DNA. Translation: AAA52757.1. M23115 mRNA. Translation: AAA53194.1. M23278, M23116 Genomic DNA. Translation: AAA52758.1. BC035588 mRNA. Translation: AAH35588.1.
IPI	IPI00177817. IPI00219078.
PIR	A31981. B31981.
RefSeq	NP_001129237.1. NP_001672.1. NP_733765.1.
UniGene	Hs.506759
3D structure databases
SMR	P16615. Positions 1-992.
ModBase	Search...
Protein-protein interaction databases
IntAct	P16615. 9 interactions.
STRING	P16615.
Protein family/group databases
TCDB	3.A.3.2.7. P-type ATPase (P-ATPase) superfamily.
PTM databases
PhosphoSite	P16615.
2-D gel databases
HSC-2DPAGE	P16614.
Proteomic databases
PRIDE	P16615.
Genome annotation databases
Ensembl	ENST00000313432; ENSP00000324892; ENSG00000174437; Homo sapiens. [Genome view]
GeneID	488.
KEGG	hsa:488.
UCSC	uc001tqk.2. human. uc001tql.2. human.
Organism-specific databases
CTD	488.
GeneCards	GC12P109182.
H-InvDB	HIX0010989.
HGNC	HGNC:812. ATP2A2.
MIM	101900. phenotype. 108740. gene. 124200. phenotype.
Orphanet	79151. Acrokeratosis verruciformis of Hopf. 218. Darier disease.
PharmGKB	PA71.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08565.
HOGENOM	HBG456486.
HOVERGEN	P16615.
InParanoid	P16615.
OMA	PNKPSRT.
PhylomeDB	P16615.
Enzyme and pathway databases
BRENDA	3.6.3.8. 247.
Gene expression databases
ArrayExpress	P16615.
Bgee	P16615.
CleanEx	HS_ATP2A2.
Genevestigator	P16615.
GermOnline	ENSG00000174437. Homo sapiens.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR005782. ATPase_P-typ_Ca-transp. IPR006068. ATPase_P-typ_cation-transptr_C. IPR004014. ATPase_P-typ_cation-transptr_N. IPR000695. ATPase_P-typ_H-transp. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR005834. Dehalogen-like_hydro. [Graphical view]
PANTHER	PTHR11939. ATPase_P. 1 hit.
Pfam	PF00689. Cation_ATPase_C. 1 hit. PF00690. Cation_ATPase_N. 1 hit. PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE. PR00120. HATPASE.
SMART	SM00831. Cation_ATPase_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR01116. ATPase-IIA1_Ca. 1 hit. TIGR01494. ATPase_P-type. 4 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	2031.
SOURCE	Search...

Entry information

Entry name

AT2A2_HUMAN

Accession

Primary (citable) accession number: P16615
Secondary accession number(s): P16614

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	February 9, 2010
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.